Immediate objectives of the proposed research are: (1) Solubilization, separation, and purification of the N-acetylglucosaminyltransferases catalyzing the biosynthesis in vitro of branched Ii-core structure using specific affinity columns from mouse lymphoma. Presence of either of these enzymes in other mouse B- and T-lymphomas and their possible roles in regulation of Ii-antigen expression on the tumors will be studied. (2) Using affinity chromatography, betaGalT-4, which catalyzes the biosynthesis in vitro of core nLcOse?4?Cer, will be separated from betaGlcNAcT and attempts will be made to further purify this betaGalT-4. Exact chemical linkage of the product of betaGalT-4-catalyzed reaction will be determined by permethylation of the product Gal-[?14?C-Ac]LcOse?3?Cer. (3) Different kinetic parameters of these enzymes (betaGlcNAcTs and betaGalT-4) will be studied after further purification of the solubilized enzymes. The major emphasis of this proposal would be to determine the possible relationship between tumorigenicity and expression of Ii-antigen in these mouse B- and T-lymphomas. (A)
| Das, K K; Basu, M; Basu, S et al. (1986) Biosynthesis in vitro of a globoside containing a 2-acetamido-2-deoxy-beta-D-galactopyranosyl group (1----3)-linked and Forssman glycolipid by two N-acetylgalactosaminyltransferases from chemically transformed guinea pig cells. Carbohydr Res 149:119-35 |
| Higashi, H; Basu, M; Basu, S (1985) Biosynthesis in vitro of disialosylneolactotetraosylceramide by a solubilized sialyltransferase from embryonic chicken brain. J Biol Chem 260:824-8 |
